Function and Biology Details
Reaction catalysed:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181990 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase A2 domain-containing protein
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.76 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.76 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
- Canonical:
Q7SSE3 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Peptidase A2 domain-containing protein
Molecule details ›
Chain: B
Length: 99 amino acids
Theoretical weight: 10.75 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.75 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
- Canonical: Q7SSI0 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
